2Q06

Crystal structure of Influenza A Virus H5N1 Nucleoprotein

Summary for 2Q06

• Entry DOI: 10.2210/pdb2q06/pdb
• Descriptor: Nucleoprotein (1 entity in total)
• Functional Keywords: influenza, h5n1, nucleoprotein, viral protein, rna binding protein
• Biological source: Influenza A virus (virus)
• Total number of polymer chains: 2
• Total formula weight: 113686.73

Authors

Ng, A.K.L.,Zhang, H.,Tan, K.,Wang, J.,Shaw, P.C. (deposition date: 2007-05-21, release date: 2008-05-27, Last modification date: 2023-08-30)

Primary citation

Ng, A.K.,Zhang, H.,Tan, K.,Li, Z.,Liu, J.H.,Chan, P.K.,Li, S.M.,Chan, W.Y.,Au, S.W.,Joachimiak, A.,Walz, T.,Wang, J.H.,Shaw, P.C.
Structure of the influenza virus A H5N1 nucleoprotein: implications for RNA binding, oligomerization, and vaccine design.
Faseb J., 22:3638-3647, 2008

PubMed Abstract: The threat of a pandemic outbreak of influenza virus A H5N1 has become a major concern worldwide. The nucleoprotein (NP) of the virus binds the RNA genome and acts as a key adaptor between the virus and the host cell. It, therefore, plays an important structural and functional role and represents an attractive drug target. Here, we report the 3.3-A crystal structure of H5N1 NP, which is composed of a head domain, a body domain, and a tail loop. Our structure resolves the important linker segments (residues 397-401, 429-437) that connect the tail loop with the remainder of the molecule and a flexible, basic loop (residues 73-91) located in an arginine-rich groove surrounding Arg150. Using surface plasmon resonance, we found the basic loop and arginine-rich groove, but mostly a protruding element containing Arg174 and Arg175, to be important in RNA binding by NP. We also used our crystal structure to build a ring-shaped assembly of nine NP subunits to model the miniribonucleoprotein particle previously visualized by electron microscopy. Our study of H5N1 NP provides insight into the oligomerization interface and the RNA-binding groove, which are attractive drug targets, and it identifies the epitopes that might be used for universal vaccine development.

PubMed: 18614582
DOI: 10.1096/fj.08-112110

Experimental method

X-RAY DIFFRACTION (3.3 Å)